Abstract:
:The carboxysomal polypeptides of Thiobacillus neapolitanus with apparent molecular masses of 85 and 130 kDa were isolated and subjected to N-terminal sequencing. The first 17 amino acids of the two peptides were identical. The sequence perfectly matched the deduced amino acid sequence of an open reading frame in the carboxysome operon. The gene was subsequently named csoS2. Expression of the gene in Escherichia coli resulted in the production of two peptides with apparent molecular masses of 85 and 130 kDa. Immunospecific antibodies generated against the smaller peptide recognized both peptides; the peptides were named CsoS2A and CsoS2B, respectively. A digoxigenin-hydrazide glycosylation assay revealed that both CsoS2A and CsoS2B are post-translationally modified by glycosylation. CsoS2 was localized to the edges of purified carboxysomes by immunogold electron microscopy using the monospecific CsoS2A antibodies. The molecular mass of CsoS2A calculated from the nucleotide sequence was 92.3 kDa.
journal_name
Arch Microbioljournal_title
Archives of microbiologyauthors
Baker SH,Lorbach SC,Rodriguez-Buey M,Williams DS,Aldrich HC,Shively JMdoi
10.1007/s002030050765keywords:
subject
Has Abstractpub_date
1999-10-01 00:00:00pages
233-9issue
4eissn
0302-8933issn
1432-072Xpii
91720233.203journal_volume
172pub_type
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